ID E3BIP3_9VIBR Unreviewed; 242 AA.
AC E3BIP3;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=Glutaredoxin {ECO:0000313|EMBL:EFP97080.1};
GN ORFNames=VIBC2010_03487 {ECO:0000313|EMBL:EFP97080.1};
OS Vibrio caribbeanicus ATCC BAA-2122.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=796620 {ECO:0000313|EMBL:EFP97080.1, ECO:0000313|Proteomes:UP000002943};
RN [1] {ECO:0000313|EMBL:EFP97080.1, ECO:0000313|Proteomes:UP000002943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2122 {ECO:0000313|EMBL:EFP97080.1,
RC ECO:0000313|Proteomes:UP000002943};
RX PubMed=21930677; DOI=10.1099/ijs.0.032375-0;
RA Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., Naum M.,
RA McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.;
RT "Vibrio caribbeanicus sp. nov., isolated from the marine sponge
RT Scleritoderma cyanea.";
RL Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFP97080.1}.
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DR EMBL; AEIU01000066; EFP97080.1; -; Genomic_DNA.
DR RefSeq; WP_009600884.1; NZ_AEIU01000066.1.
DR AlphaFoldDB; E3BIP3; -.
DR STRING; 796620.VIBC2010_03487; -.
DR eggNOG; COG0678; Bacteria.
DR eggNOG; COG0695; Bacteria.
DR OrthoDB; 9800621at2; -.
DR Proteomes; UP000002943; Unassembled WGS sequence.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:InterPro.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:InterPro.
DR CDD; cd03013; PRX5_like; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR InterPro; IPR011767; GLR_AS.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR011906; Glutaredoxin_dom.
DR InterPro; IPR014025; Glutaredoxin_subgr.
DR InterPro; IPR037944; PRX5-like.
DR InterPro; IPR013740; Redoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR02190; GlrX-dom; 1.
DR PANTHER; PTHR10430; PEROXIREDOXIN; 1.
DR PANTHER; PTHR10430:SF16; PEROXIREDOXIN-5, MITOCHONDRIAL; 1.
DR Pfam; PF00462; Glutaredoxin; 1.
DR Pfam; PF08534; Redoxin; 1.
DR PRINTS; PR00160; GLUTAREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000002943}.
FT DOMAIN 4..168
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 50
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR637944-1"
SQ SEQUENCE 242 AA; 27024 MW; BBA12C144359D601 CRC64;
MFSSKEGQHI PQVTFPTRQG DAWVNVTTDE LFKDKTVIVF SLPGAFTPTC SSTHLPRYNE
LFSVFKEHGV DEIVCVSVND TFVMNAWKND QEADNIRFIP DGNGEFTQGM GMLADKNDIG
FGQRSWRYSM LVKNGLIEKM FIEPNEPGDP FKVSDADTML KYIAPEYKTQ ESITVFTKPG
CPFCAKAKQS LIDHELQYEE VVLGKDATTV SLRAISGRTT VPQVFVGGKH IGGSEELDNY
LS
//
